Microstructural kinetic properties of small molecules and proteins will be investigated using magnetic resonance. Particular problems being considered are: (1) Hemoglobin: Kinetics of oxygen ligation and of tertiary conformation change, and their relationship to cooperativity. (2) Nucleic acids: Conformational stability as monitored by exchange rates with solvent of base pair protons, and by nuclear spin relaxation rates. (3) Structure of enzymes as inferred from their perturbation on NMR relaxation rates of small molecules and of the electronic structure of cytochrome c. These problems will be attacked by double nuclear magnetic resonance, high sensitivity nuclear quadrupole resonance. A major interest is instrumentation for NMR observations of protons of solutes in H2O.